2011•AmyloidRequires access

Antioxidative effect of albumin on amyloid fibril formation in transthyretin-related amyloidosis

Jianying Guo, Hirofumi Jono, Tomoe Kugimiya, Setsuko Saito, T. Maruyama, Yohei Misumi, Yoshinobu Hoshii, Y. Su, Mamiko Shono, Mitsuharu Ueda, Konen Obayashi, Masaki Otagiri, Yukio Ando

Open publisher page 8 citations

Abstract

Abstract: Transthyretin (TTR)-related familial amyloidotic polyneuropathy (FAP) is characterized by systemic accumulation of amyloid fibrils caused by a point mutation in the TTR gene. Despite the ...

About this research paper

What this paper is about

Abstract: Transthyretin (TTR)-related familial amyloidotic polyneuropathy (FAP) is characterized by systemic accumulation of amyloid fibrils caused by a point mutation in the TTR gene. Despite the ...

Why it matters

OpenAlex reports 8 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

Abstract: Transthyretin (TTR)-related familial amyloidotic polyneuropathy (FAP) is characterized by systemic accumulation of amyloid fibrils caused by a point mutation in the TTR gene. Despite the ...

Key concepts: Transthyretin, Amyloidosis, Polyneuropathy, Amyloid fibril, Amyloid (mycology), Amyloid polyneuropathy, Albumin, Point mutation

Related papers

Back to paper searchBrowse research topicsOriginal source
Antioxidative effect of albumin on amyloid fibril formation in transthyretin-related amyloidosis — Research Paper | ScholarLens